IF2_LISMO
ID IF2_LISMO Reviewed; 779 AA.
AC Q8Y7F6;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=lmo1325;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; AL591978; CAC99403.1; -; Genomic_DNA.
DR PIR; AE1240; AE1240.
DR RefSeq; NP_464850.1; NC_003210.1.
DR RefSeq; WP_010990095.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y7F6; -.
DR SMR; Q8Y7F6; -.
DR STRING; 169963.lmo1325; -.
DR PaxDb; Q8Y7F6; -.
DR EnsemblBacteria; CAC99403; CAC99403; CAC99403.
DR GeneID; 987704; -.
DR KEGG; lmo:lmo1325; -.
DR PATRIC; fig|169963.11.peg.1362; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; Q8Y7F6; -.
DR BioCyc; LMON169963:LMO1325-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..779
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137219"
FT DOMAIN 280..449
FT /note="tr-type G"
FT REGION 44..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..296
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 314..318
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 335..338
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 389..392
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 425..427
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289..296
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 335..339
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 389..392
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 779 AA; 84576 MW; B377A8DC28294AFF CRC64;
MSKVRVYEYA KEHQVSSKKV IEALKDLGIE VANHMSTINE NALRQLDNAV DGTNKKAEAP
KKETTSNENG NSKGPNKPNM TNSNEKSNKP NKPAGQANKP ATANKSQGAK PATNKPANTS
NQTQSSGTQQ QAGGQKRNNS NRPGGGNSNR PGGNNRPNRG GNFNNKGRNT KKKGKLNHST
VPPTPPKPKE LPEKIVFSES LTVAELAKKL YREPSELIKK LFMLGVVATI NQSLDKDAIE
LICDDYGVQV EEEIKVDVTD LDVYFENELN EAVDESKLVE RPPVVTIMGH VDHGKTTLLD
SLRNTKVTLG EAGGITQHIG AYQLEIHDKK ITFLDTPGHA AFTAMRARGA QITDITILVV
AADDGVMPQT IEAINHAKAA GMPIIVAVNK IDKPQANPDR VMQELTEYEL VPEAWGGDTI
FAPISAKFGE GLENLLDMIL LVSEVEELKA NPDRRAIGSV IEAELDKGRG PVATLLVQDG
TLNIGDPIVV GNTFGRVRAM VNDLGRRVKK VGPSTPVEIT GLNDVPQAGD RFVVFEDEKT
ARNIGETRAS RALVAQRSAT NRVSLDNLFE HMKAGEMKEV NVIIKADVQG SVEALAASLR
KIDVEGVNVK IIHTAVGAIN ESDITLAAAS NAIVIGFNVR PTAQAREAAE NESVDIRLHR
VIYKAIDEIE AAMKGMLDPE FQEKIIGQAQ VRQTINVSKV GTIAGCYVTD GKITRDSGVR
IIRDGIVVFE GEIATLKRFK DDAKEVAKGY ECGITVQNFN DIKEDDVIEA YVMEEIERK
